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Multiple Domains Within the Cauliflower mosaic virus Gene VI Product Interact with the Full-Length Protein

October 2002 , Volume 15 , Number  10
Pages  1,050 - 1,057

Yongzhong Li and Scott M. Leisner

Department of Biological Sciences, The University of Toledo, 2801 West Bancroft Street, Toledo, OH 43606, U.S.A.

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Accepted 10 June 2002.

The Cauliflower mosaic virus (CaMV) gene VI product (P6) is a multifunctional protein essential for viral propagation. It is likely that at least some of these functions require P6 self-association. The work described here was performed to confirm that P6 self-associates and to identify domains involved in this interaction. Yeast two-hybrid analyses indicated that full-length P6 self-associates and that this interaction is specific. Additional analyses indicated that at least four independent domains bind to full-length P6. When a central domain (termed domain D3) was removed, these interactions were abolished. However, this deleted P6 was able to bind to the full-length wild-type protein and to isolated domain D3. Viruses lacking domain D3 were incapable of producing a systemic infection. Isolated domain D3 was capable of binding to at least two of the other domains but was unable to self-associate. This suggests that domain D3 facilitates P6 self-association by binding to the other domains but not itself. The presence of multiple domains involved in P6 self-association may help explain the ability of this protein to form the intracellular inclusions characteristic of caulimoviruses.

Additional keywords: viroplasm , translational transactivation.

© 2002 The American Phytopathological Society